Funds are requested for the acquisition of a liquid state 14.1 T NMR spectrometer to be used by a group of scientists from the Chemistry Department and the Biochemistry and Molecular Biology Department of The Pennsylvania State University. This instrument would update and expand the capabilities available within the Nuclear Magnetic Resonance Facility of the Chemistry Department. The primary investigators are all currently involved in projects that require the collection of high-resolution data on proteins in solution. A short description of their research interests follows. Stephen J. Benkovic - Investigation of the factors underlying catalysis and substrate binding in several classes of enzymes: catalytic antibodies, DNA polymerase I, T4 polymerase complex, dihydrofolate reductase, and trifunctional enzymes in the de novo pathway for purine biosynthesis. Donald A. Bryant - Molecular biology and biochemistry in photosynthetic apparatus from cyanobacteria and green bacteria; mechanism of electron transport of cyanobacteria; structure-function relationships in photosystem I; origins of chloroplasts. Christopher J. Falzone - Solution structure of proteins using multinuclear and multidimensional NMR methods; backbone dynamics; substrate dynamics and the effects of site-directed mutation on substrate specificity and protein structure. Juliette T. J. Lecomte - Structure and dynamics of partially folded proteins in solution; determinants of structure in small water-soluble proteins; modulation of structural and thermodynamic properties by specific and non-specific salt effects. C. Robert Matthews - Mechanism by which the primary structure of a protein directs the rapid and efficient folding to the native conformation; site- directed mutagenesis to target individual amino acids in the alpha subunit of tryptophan synthase, dihydrofolate reductase, and ras p2l. With the new instrument, these investigators and a group of several secondary investigators will be in a position to engage in and carry out competitive research related to structure and function in biological systems. The availability of a 14.1 T spectrometer will also allow other researchers to access the currently overbooked 11.7 T instrument.